메뉴 건너뛰기




Volumn 23, Issue 5, 2007, Pages 1254-1257

Molecularly imprinted polymer-assisted refolding of lysozyme

Author keywords

[No Author keywords available]

Indexed keywords

ACRYLICS; BINDING ENERGY; DENATURATION; POLYMERS;

EID: 35348853714     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp070130c     Document Type: Article
Times cited : (21)

References (23)
  • 1
    • 14744269790 scopus 로고
    • Structure and morphology of protein inclusion bodies in Escherichia coli
    • Bowden, G. A.; Paredes, A. M.; Georgiou, G. Structure and morphology of protein inclusion bodies in Escherichia coli. Bio/Technology 1991, 58, 725-730.
    • (1991) Bio/Technology , vol.58 , pp. 725-730
    • Bowden, G.A.1    Paredes, A.M.2    Georgiou, G.3
  • 2
    • 0029136831 scopus 로고
    • Artificial chaperones - protein refolding via sequential use of detergent and cyclodextrin
    • Rozema, D.; Gellman, S. H. Artificial chaperones - protein refolding via sequential use of detergent and cyclodextrin. J. Am. Chem. Soc. 1995, 117, 2373-2374.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 2373-2374
    • Rozema, D.1    Gellman, S.H.2
  • 3
    • 0029774156 scopus 로고    scopus 로고
    • Artificial chaperone-assisted refolding of denatured-reduced lysozyme: Modulation of the competition between renaturation and aggregation
    • Rozema, D.; Gellman, S. H. Artificial chaperone-assisted refolding of denatured-reduced lysozyme: modulation of the competition between renaturation and aggregation. Biochemistry 1996, 35, 15760-15771.
    • (1996) Biochemistry , vol.35 , pp. 15760-15771
    • Rozema, D.1    Gellman, S.H.2
  • 6
    • 0006454079 scopus 로고
    • Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli
    • Buchner, J.; Rudolph, R. Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Bio/Technology 1991, 9, 157-162.
    • (1991) Bio/Technology , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 7
    • 0032191701 scopus 로고    scopus 로고
    • Highly efficient recovery of functional single-chain Fv fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagent - application to a human single-chain Fv fragment
    • Tsumoto, K.; Shinoki, K.; Kondo, H.; Uchikawa, M.; Juji, T.; Kumagai, I. Highly efficient recovery of functional single-chain Fv fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagent - application to a human single-chain Fv fragment. J. Immunol. Methods 1998, 219, 119-129.
    • (1998) J. Immunol. Methods , vol.219 , pp. 119-129
    • Tsumoto, K.1    Shinoki, K.2    Kondo, H.3    Uchikawa, M.4    Juji, T.5    Kumagai, I.6
  • 8
    • 15244343628 scopus 로고    scopus 로고
    • L-Arginine increases the solubility of unfolded species of hen egg white lysozyme
    • Reddy K., R. C.; Lilie, H.; Rudolph, R.; Lange, C. L-Arginine increases the solubility of unfolded species of hen egg white lysozyme. Protein Sci. 2005, 14, 929-935.
    • (2005) Protein Sci , vol.14 , pp. 929-935
    • Reddy, K.R.C.1    Lilie, H.2    Rudolph, R.3    Lange, C.4
  • 9
    • 0344442884 scopus 로고    scopus 로고
    • Prevention of thermal inactivation and aggregation of lysozyme by polyamines
    • Kudou, M.; Shiraki, K.; Fujiwara, S.; Imanaka, T.; Takagi, M. Prevention of thermal inactivation and aggregation of lysozyme by polyamines. Eur. J. Biochem. 2003, 270, 4547-4554.
    • (2003) Eur. J. Biochem , vol.270 , pp. 4547-4554
    • Kudou, M.1    Shiraki, K.2    Fujiwara, S.3    Imanaka, T.4    Takagi, M.5
  • 10
    • 33646286416 scopus 로고    scopus 로고
    • Hsp47: A collagen-specific molecular chaperone
    • Nagata, K. Hsp47: a collagen-specific molecular chaperone. Trends Biochem. Sci. 1996, 21, 22-26.
    • (1996) Trends Biochem. Sci , vol.21 , pp. 22-26
    • Nagata, K.1
  • 11
    • 0035910560 scopus 로고    scopus 로고
    • The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli
    • Silberg, J. J.; Hoff, K. G.; Tapley, T. L.; Vickery, L. E. The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli. J. Biol. Chem. 2001, 276, 1696-1700.
    • (2001) J. Biol. Chem , vol.276 , pp. 1696-1700
    • Silberg, J.J.1    Hoff, K.G.2    Tapley, T.L.3    Vickery, L.E.4
  • 13
    • 0027415107 scopus 로고
    • The role of binding-site interactions in the molecular imprinting of polymers
    • Wulff, G. The role of binding-site interactions in the molecular imprinting of polymers. Trends Biotechnol. 1993, 11, 85-87.
    • (1993) Trends Biotechnol , vol.11 , pp. 85-87
    • Wulff, G.1
  • 14
    • 0027983036 scopus 로고
    • Molecular imprinting
    • Mosbach, K. Molecular imprinting. Trends Biochem. Sci. 1994, 19, 9-14.
    • (1994) Trends Biochem. Sci , vol.19 , pp. 9-14
    • Mosbach, K.1
  • 15
    • 0035968652 scopus 로고    scopus 로고
    • Synthesis of polymer particles with specific lysozyme recognition sites by a molecular imprinting technique
    • Hirayama, K.; Sakai, Y.; Kameoka, K. Synthesis of polymer particles with specific lysozyme recognition sites by a molecular imprinting technique. J. Appl. Polym. Sci. 2001, 81, 3378-3387.
    • (2001) J. Appl. Polym. Sci , vol.81 , pp. 3378-3387
    • Hirayama, K.1    Sakai, Y.2    Kameoka, K.3
  • 16
    • 1642493677 scopus 로고    scopus 로고
    • Polyacrylamide gels with electrostatic functional groups for the molecular imprinting of lysozyme
    • Ou, S. H.; Wu, M. C.; Chou, T. C.; Liu, C. C. Polyacrylamide gels with electrostatic functional groups for the molecular imprinting of lysozyme. Anal. Chim. Acta 2004, 504, 163-166.
    • (2004) Anal. Chim. Acta , vol.504 , pp. 163-166
    • Ou, S.H.1    Wu, M.C.2    Chou, T.C.3    Liu, C.C.4
  • 17
    • 34249898032 scopus 로고    scopus 로고
    • Study of the interactions between protein-imprinted hydrogels and their templates
    • Kimhi, O.; Bianco-Peled, H. Study of the interactions between protein-imprinted hydrogels and their templates. Langmuir 2007, 23, 6329-6335.
    • (2007) Langmuir , vol.23 , pp. 6329-6335
    • Kimhi, O.1    Bianco-Peled, H.2
  • 18
    • 0035499853 scopus 로고    scopus 로고
    • Surface-grafted molecularly imprinted polymers for protein recognition
    • Bossi, A.; Piletsky, S. A.; Piletska, E. V.; Righetti, P. G.; Turner, A. P. F. Surface-grafted molecularly imprinted polymers for protein recognition. Anal. Chem. 2001, 73, 5281-5286.
    • (2001) Anal. Chem , vol.73 , pp. 5281-5286
    • Bossi, A.1    Piletsky, S.A.2    Piletska, E.V.3    Righetti, P.G.4    Turner, A.P.F.5
  • 19
    • 33749242388 scopus 로고    scopus 로고
    • The microcontact imprinting of proteins: The effect of cross-linking monomers for lysozyme, ribonuclease A and myoglobin
    • Lin, H. Y.; Hsu, C. Y.; Thomas, J. L.; Wang, S. E.; Chen, H. C.; Chou, T. C. The microcontact imprinting of proteins: The effect of cross-linking monomers for lysozyme, ribonuclease A and myoglobin. Biosens. Bioelectron. 2006, 22, 534-543.
    • (2006) Biosens. Bioelectron , vol.22 , pp. 534-543
    • Lin, H.Y.1    Hsu, C.Y.2    Thomas, J.L.3    Wang, S.E.4    Chen, H.C.5    Chou, T.C.6
  • 20
    • 0032898359 scopus 로고    scopus 로고
    • Effect of acrylamide on aldolase structure. II. Characterization of aldolase unfolding intermediates
    • Dobryszycki, P.; Rymarczuk, M.; Gapinski, J.; Kochman, M. Effect of acrylamide on aldolase structure. II. Characterization of aldolase unfolding intermediates. Biochim. Biophys. Acta. 1999, 1431, 351-362.
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 351-362
    • Dobryszycki, P.1    Rymarczuk, M.2    Gapinski, J.3    Kochman, M.4
  • 21
    • 0014937559 scopus 로고
    • Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme
    • Saxena, V. P.; Wetlaufer, D. B. Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme. Biochemistry 1970, 9, 5015-5023.
    • (1970) Biochemistry , vol.9 , pp. 5015-5023
    • Saxena, V.P.1    Wetlaufer, D.B.2
  • 22
    • 0035913902 scopus 로고    scopus 로고
    • Dual function of protein confinement in chaperonin-assisted protein folding
    • Brinker, A.; Pfeifer, G.; Kerner, M. L.; Naylor, D. J.; Hartl, F. U.; Hayer-Hartl, M. Dual function of protein confinement in chaperonin-assisted protein folding. Cell 2001, 107, 223-233.
    • (2001) Cell , vol.107 , pp. 223-233
    • Brinker, A.1    Pfeifer, G.2    Kerner, M.L.3    Naylor, D.J.4    Hartl, F.U.5    Hayer-Hartl, M.6
  • 23
    • 30444458726 scopus 로고    scopus 로고
    • Monte Carlo simulation of protein folding in the presence of residue-specific binding sites
    • Rossinsky, E.; Srebnik, S. Monte Carlo simulation of protein folding in the presence of residue-specific binding sites. Biopolymers 2005, 79, 259-268.
    • (2005) Biopolymers , vol.79 , pp. 259-268
    • Rossinsky, E.1    Srebnik, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.